SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B7URX9

- PDXH_ECO27

UniProt

B7URX9 - PDXH_ECO27

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Pyridoxine/pyridoxamine 5'-phosphate oxidase
Gene
pdxH, E2348C_1725
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.UniRule annotation

Catalytic activityi

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.UniRule annotation
Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.UniRule annotation

Cofactori

Binds 1 FMN per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671FMN By similarity
Binding sitei70 – 701FMN; via amide nitrogen By similarity
Binding sitei72 – 721Substrate By similarity
Binding sitei89 – 891FMN By similarity
Binding sitei129 – 1291Substrate By similarity
Binding sitei133 – 1331Substrate By similarity
Binding sitei137 – 1371Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi82 – 832FMN By similarity
Nucleotide bindingi146 – 1472FMN By similarity

GO - Molecular functioni

  1. FMN binding Source: UniProtKB-HAMAP
  2. pyridoxamine-phosphate oxidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pyridoxine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciECOL574521:GJAO-1779-MONOMER.
UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC:1.4.3.5)
Alternative name(s):
PNP/PMP oxidase
Short name:
PNPOx
Pyridoxal 5'-phosphate synthase
Gene namesi
Name:pdxH
Ordered Locus Names:E2348C_1725
OrganismiEscherichia coli O127:H6 (strain E2348/69 / EPEC)
Taxonomic identifieri574521 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008205: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Pyridoxine/pyridoxamine 5'-phosphate oxidaseUniRule annotation
PRO_1000186304Add
BLAST

Proteomic databases

PRIDEiB7URX9.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi574521.E2348C_1725.

Structurei

3D structure databases

ProteinModelPortaliB7URX9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 174Substrate binding By similarity
Regioni197 – 1993Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0259.
KOiK00275.
OMAiNMGSRKA.
OrthoDBiEOG60KN2Z.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851. PTHR10851. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B7URX9-1 [UniParc]FASTAAdd to Basket

« Hide

MSDNDELQQI AHLRREYTKG GLRRRDLPAD PLTLFERWLS QACEAKLADP    50
TAMVVATVDE HGQPYQRIVL LKHYDEKGMV FYTNLGSRKA HQIENNPRVS 100
LLFPWHTLER QVMVIGKAER LSTLEVMKYF HSRPRDSQIG AWVSKQSSRI 150
SARGILESKF LELKQKFQQG EVPLPSFWGG FRVSLEQIEF WQGGEHRLHD 200
RFLYQRENDA WKIDRLAP 218
Length:218
Mass (Da):25,545
Last modified:February 10, 2009 - v1
Checksum:i8B47CEEEA6CEF5F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM180568 Genomic DNA. Translation: CAS09273.1.
RefSeqiYP_002329246.1. NC_011601.1.

Genome annotation databases

EnsemblBacteriaiCAS09273; CAS09273; E2348C_1725.
GeneIDi7062287.
KEGGiecg:E2348C_1725.
PATRICi18342465. VBIEscCol90278_1759.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM180568 Genomic DNA. Translation: CAS09273.1 .
RefSeqi YP_002329246.1. NC_011601.1.

3D structure databases

ProteinModelPortali B7URX9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 574521.E2348C_1725.

Proteomic databases

PRIDEi B7URX9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAS09273 ; CAS09273 ; E2348C_1725 .
GeneIDi 7062287.
KEGGi ecg:E2348C_1725.
PATRICi 18342465. VBIEscCol90278_1759.

Phylogenomic databases

eggNOGi COG0259.
KOi K00275.
OMAi NMGSRKA.
OrthoDBi EOG60KN2Z.

Enzyme and pathway databases

UniPathwayi UPA00190 ; UER00304 .
UPA00190 ; UER00305 .
BioCyci ECOL574521:GJAO-1779-MONOMER.

Family and domain databases

Gene3Di 2.30.110.10. 1 hit.
HAMAPi MF_01629. PdxH.
InterProi IPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view ]
PANTHERi PTHR10851. PTHR10851. 1 hit.
Pfami PF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMi SSF50475. SSF50475. 1 hit.
TIGRFAMsi TIGR00558. pdxH. 1 hit.
PROSITEi PS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
    Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
    J. Bacteriol. 191:347-354(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E2348/69 / EPEC.

Entry informationi

Entry nameiPDXH_ECO27
AccessioniPrimary (citable) accession number: B7URX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: June 11, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi